Infrared spectroscopic characterization of the structural changes connected with the E1→E2 transition in the Ca2+-ATPase of sarcoplasmic reticulum.
Open Access
- 1 July 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (19) , 9037-9043
- https://doi.org/10.1016/s0021-9258(18)48043-x
Abstract
No abstract availableThis publication has 44 references indexed in Scilit:
- Image Analysis of the Ca2+-ATPase from Sarcoplasmic ReticulumAnnals of the New York Academy of Sciences, 1986
- A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease SBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequencesCell, 1986
- Three-dimensional reconstruction of negatively stained crystals of the Ca2+-ATPase from muscle sarcoplasmic reticulumJournal of Molecular Biology, 1986
- Retention of ellipticity between enzymatic states of the Ca2+‐ATPase of sarcoplasmic reticulumFEBS Letters, 1986
- Fourier transform infrared spectroscopic studies of the secondary structure and thermal denaturation of CaATPase from rabbit skeletal muscleSpectrochimica Acta Part A: Molecular Spectroscopy, 1986
- Polymorphic phase behaviour of phospholipid membranes studied by infrared spectroscopyBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1984
- Fourier transform infrared spectroscopic studies of lipid-protein interaction in native and reconstituted sarcoplasmic reticulumBiochimica et Biophysica Acta (BBA) - Biomembranes, 1984
- Vibrational assignment of the sn-1 and sn-2 chain carbonyl stretching modes of membrane phospholipidsJournal of Raman Spectroscopy, 1982
- Intrinsic protein-lipid interactionsJournal of Molecular Biology, 1982